(data stored in ACNUC7421 zone)

SWISSPROT: MHPB_SHISS

ID   MHPB_SHISS              Reviewed;         314 AA.
AC   Q3Z586;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
DE            EC=1.13.11.16 {ECO:0000255|HAMAP-Rule:MF_01653};
DE   AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
GN   Name=mhpB {ECO:0000255|HAMAP-Rule:MF_01653};
GN   OrderedLocusNames=SSON_0295;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative
CC       cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-
CC       dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-
CC       hydroxy-6-ketononatrienedioate, respectively. {ECO:0000255|HAMAP-
CC       Rule:MF_01653}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-
CC         hydroxy-6-oxonona-2,4-dienedioate + H(+); Xref=Rhea:RHEA:23840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:46951,
CC         ChEBI:CHEBI:66887; EC=1.13.11.16; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01653};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 =
CC         (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H(+);
CC         Xref=Rhea:RHEA:25054, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:58642, ChEBI:CHEBI:66888; EC=1.13.11.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01653};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01653};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_01653}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01653}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01653}.
DR   EMBL; CP000038; AAZ87076.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87076; AAZ87076; SSON_0295.
DR   KEGG; ssn:SSON_0295; -.
DR   HOGENOM; HOG000069851; -.
DR   KO; K05713; -.
DR   OMA; RTWIAAF; -.
DR   BioCyc; SSON300269:G1GL2-341-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07365; MhpB_like; 1.
DR   HAMAP; MF_01653; MhpB; 1.
DR   InterPro; IPR023789; DHPP/DHXA_dioxygenase.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z586.
DR   SWISS-2DPAGE; Q3Z586.
KW   Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase;
KW   Iron; Oxidoreductase.
FT   CHAIN         1    314       2,3-dihydroxyphenylpropionate/2,3-
FT                                dihydroxicinnamic acid 1,2-dioxygenase.
FT                                /FTId=PRO_0000337669.
FT   ACT_SITE    115    115       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01653}.
FT   ACT_SITE    179    179       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01653}.
SQ   SEQUENCE   314 AA;  34196 MW;  E1D5A8574E5DFE05 CRC64;
     MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD
     VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP
     LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ
     PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ
     FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE
     WIAGFGSLSA RTEN
//

If you have problems or comments...

PBIL Back to PBIL home page